BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50147

Title: 1H, 15N, and 13C backbone chemical shift assignments for the second bromodomain of BRD3 (BRD3-BD2)   PubMed: 33620209

Deposition date: 2019-12-31 Original release date: 2021-08-12

Authors: Patel, Karishma; Mackay, Joel; Solomon, Paul

Citation: Patel, Karishma; Solomon, Paul; Walshe, James; Ford, Daniel; Wilkinson-White, Lorna; Payne, Richard; Low, Jason; Mackay, Joel. "BET-Family Bromodomains Can Recognize Diacetylated Sequences from Transcription Factors Using a Conserved Mechanism"  Biochemistry 60, 648-662 (2021).

Assembly members:
The second bromodomain of BRD3, polymer, 118 residues, Formula weight is not available

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P

Entity Sequences (FASTA):
The second bromodomain of BRD3: GPLGSKLSEHLRYCDSILRE MLSKKHAAYAWPFYKPVDAE ALELHDYHDIIKHPMDLSTV KRKMDGREYPDAQGFAADVR LMFSNCYKYNPPDHEVVAMA RKLQDVFEMRFAKMPDEP

Data sets:
Data typeCount
13C chemical shifts129
15N chemical shifts62
1H chemical shifts62

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1The second bromodomain of BRD31

Entities:

Entity 1, The second bromodomain of BRD3 118 residues - Formula weight is not available

1   GLYPROLEUGLYSERLYSLEUSERGLUHIS
2   LEUARGTYRCYSASPSERILELEUARGGLU
3   METLEUSERLYSLYSHISALAALATYRALA
4   TRPPROPHETYRLYSPROVALASPALAGLU
5   ALALEUGLULEUHISASPTYRHISASPILE
6   ILELYSHISPROMETASPLEUSERTHRVAL
7   LYSARGLYSMETASPGLYARGGLUTYRPRO
8   ASPALAGLNGLYPHEALAALAASPVALARG
9   LEUMETPHESERASNCYSTYRLYSTYRASN
10   PROPROASPHISGLUVALVALALAMETALA
11   ARGLYSLEUGLNASPVALPHEGLUMETARG
12   PHEALALYSMETPROASPGLUPRO

Samples:

sample_1: DSS 0.01 mM; TRIS 10 mM; sodium chloride 100 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts